HEADER TRANSFERASE 27-APR-07 2UZE
TITLE CRYSTAL STRUCTURE OF HUMAN CDK2 COMPLEXED WITH A
TITLE 2 THIAZOLIDINONE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: P33 PROTEIN KINASE, CYCLIN DEPENDENT KINASE 2;
COMPND 5 EC: 2.7.11.22, 2.7.1.37;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: THR160 PHOSPHORYLATED;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CYCLIN A2;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: RESIDUES 175-432;
COMPND 12 SYNONYM: CYCLIN-A;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PGEX;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR: PET41A
KEYWDS TRANSFERASE, ATP-BINDING, PHOSPHORYLATION, CDK2, KINASE,
KEYWDS 2 CYCLIN, MITOSIS, CELL CYCLE, CELL DIVISION, NUCLEOTIDE-
KEYWDS 3 BINDING, SERINE/THREONINE-PROTEIN KINASE, THIAZOLIDINONE
KEYWDS 4 LIGAND
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.RICHARDSON,P.DOKURNO,J.B.MURRAY,A.E.SURGENOR
REVDAT 3 24-FEB-09 2UZE 1 VERSN
REVDAT 2 03-JUL-07 2UZE 1 JRNL
REVDAT 1 26-JUN-07 2UZE 0
JRNL AUTH C.M.RICHARDSON,C.L.NUNNS,D.S.WILLIAMSON,
JRNL AUTH 2 M.J.PARRATT,P.DOKURNO,R.HOWES,J.BORGOGNONI,
JRNL AUTH 3 M.J.DRYSDALE,H.FINCH,R.E.HUBBARD,P.S.JACKSON,
JRNL AUTH 4 P.KIERSTAN,G.LENTZEN,J.D.MOORE,J.B.MURRAY,
JRNL AUTH 5 H.SIMMONITE,A.E.SURGENOR,C.J.TORRANCE
JRNL TITL DISCOVERY OF A POTENT CDK2 INHIBITOR WITH A NOVEL
JRNL TITL 2 BINDING MODE, USING VIRTUAL SCREENING AND INITIAL,
JRNL TITL 3 STRUCTURE-GUIDED LEAD SCOPING.
JRNL REF BIOORG.MED.CHEM.LETT. V. 17 3880 2007
JRNL REFN ISSN 0960-894X
JRNL PMID 17570665
JRNL DOI 10.1016/J.BMCL.2007.04.110
REMARK 2
REMARK 2 RESOLUTION. 2.4 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.5
REMARK 3 NUMBER OF REFLECTIONS : 60675
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3234
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3676
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 192
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8894
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 296
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.33000
REMARK 3 B22 (A**2) : -1.44000
REMARK 3 B33 (A**2) : 0.81000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.23000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.311
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.241
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.158
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.659
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9188 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12486 ; 1.733 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1104 ; 6.625 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 391 ;42.857 ;23.964
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1606 ;18.379 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;20.723 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1408 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6857 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4135 ; 0.218 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6236 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 408 ; 0.176 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 51 ; 0.224 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.231 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5707 ; 0.965 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9029 ; 1.697 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3958 ; 2.449 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3457 ; 3.777 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 999 4
REMARK 3 1 D 1 D 999 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 B (A): 2084 ; 0.21 ; 0.50
REMARK 3 MEDIUM THERMAL 1 B (A**2): 2084 ; 0.64 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2UZE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-APR-07.
REMARK 100 THE PDBE ID CODE IS EBI-32387.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUL-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70622
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.5
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOUR DIFFUSION AT 4 DEG C,
REMARK 280 0.1 M HEPES PH 7.0, 1M LITHIUM SULPHATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 106.31300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.71800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 106.31300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.71800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ARG A 297
REMARK 465 LEU A 298
REMARK 465 LEU C 298
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 THR A 39 OG1 CG2
REMARK 470 GLU A 40 CG CD OE1 OE2
REMARK 470 ARG A 199 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 38 CG OD1 OD2
REMARK 470 THR C 39 OG1 CG2
REMARK 470 ARG C 297 CA C O CB CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CG2 VAL C 64 - O HOH C 2016 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 177 CB CYS A 177 SG -0.156
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 78 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG A 150 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 150 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG C 150 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG C 150 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 8 143.16 -174.50
REMARK 500 GLU A 40 0.56 97.79
REMARK 500 THR A 41 -124.83 -166.98
REMARK 500 LEU A 58 65.32 -113.28
REMARK 500 ASP A 127 41.09 -150.17
REMARK 500 ASP A 145 78.89 53.98
REMARK 500 GLU A 162 66.48 -66.26
REMARK 500 VAL A 164 131.74 76.85
REMARK 500 SER A 181 -142.89 -144.34
REMARK 500 ARG A 199 -2.23 76.28
REMARK 500 TRP A 227 89.75 -152.19
REMARK 500 HIS A 295 35.89 -79.84
REMARK 500 PRO B 176 -159.66 -98.06
REMARK 500 PHE B 304 15.79 58.86
REMARK 500 TRP B 372 115.12 -29.79
REMARK 500 GLU C 8 145.70 -176.43
REMARK 500 THR C 39 -2.48 56.94
REMARK 500 GLU C 40 -78.86 -142.74
REMARK 500 THR C 41 -66.42 -91.71
REMARK 500 LEU C 58 64.91 -117.87
REMARK 500 ASP C 127 48.64 -152.60
REMARK 500 ASP C 145 75.33 57.61
REMARK 500 VAL C 164 131.30 72.87
REMARK 500 SER C 181 -142.81 -136.19
REMARK 500 ARG C 199 -25.82 95.14
REMARK 500 PRO C 254 -7.60 -59.40
REMARK 500 LYS C 291 78.66 -118.67
REMARK 500 PRO D 176 -160.61 -66.54
REMARK 500 TRP D 372 109.67 -33.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 38 THR A 39 126.78
REMARK 500 GLU C 40 THR C 41 -149.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU A 42 23.7 L L OUTSIDE RANGE
REMARK 500 ARG A 122 24.8 L L OUTSIDE RANGE
REMARK 500 TPO A 160 24.2 L L OUTSIDE RANGE
REMARK 500 ILE D 281 24.2 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C95 A1297
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C95 C1297
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E9H RELATED DB: PDB
REMARK 900 THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN
REMARK 900 A3 COMPLEX WITH THE INHIBITOR INDIRUBIN-5-
REMARK 900 SULPHONATE BOUND
REMARK 900 RELATED ID: 1FIN RELATED DB: PDB
REMARK 900 CYCLIN A - CYCLIN-DEPENDENT KINASE 2 COMPLEX
REMARK 900 RELATED ID: 1FVV RELATED DB: PDB
REMARK 900 THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX
REMARK 900 WITH AN OXINDOLEINHIBITOR
REMARK 900 RELATED ID: 1GY3 RELATED DB: PDB
REMARK 900 PCDK2/CYCLIN A IN COMPLEX WITH MGADP,
REMARK 900 NITRATE AND PEPTIDE SUBSTRATE
REMARK 900 RELATED ID: 1H1P RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH THE INHIBITOR NU2058
REMARK 900 RELATED ID: 1H1Q RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH THE INHIBITOR NU6094
REMARK 900 RELATED ID: 1H1R RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH THE INHIBITOR NU6086
REMARK 900 RELATED ID: 1H1S RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH THE INHIBITOR NU6102
REMARK 900 RELATED ID: 1H24 RELATED DB: PDB
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH A 9 RESIDUE
REMARK 900 RECRUITMENT PEPTIDE FROM E2F
REMARK 900 RELATED ID: 1H25 RELATED DB: PDB
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE
REMARK 900 RECRUITMENT PEPTIDE FROM E2F
REMARK 900 RELATED ID: 1H26 RELATED DB: PDB
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE
REMARK 900 RECRUITMENT PEPTIDE FROM P53
REMARK 900 RELATED ID: 1H27 RELATED DB: PDB
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE
REMARK 900 RECRUITMENT PEPTIDE FROM P27
REMARK 900 RELATED ID: 1H28 RELATED DB: PDB
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE
REMARK 900 RECRUITMENT PEPTIDE FROM P107
REMARK 900 RELATED ID: 1JST RELATED DB: PDB
REMARK 900 PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND
REMARK 900 TO CYCLIN A
REMARK 900 RELATED ID: 1JSU RELATED DB: PDB
REMARK 900 P27(KIP1)/CYCLIN A/CDK2 COMPLEX
REMARK 900 RELATED ID: 1OGU RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH A 2-ARYLAMINO-4-
REMARK 900 CYCLOHEXYLMETHYL-5-NITROSO-6-AMINOPYRIMIDINE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 1OI9 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH A 6-
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR
REMARK 900 RELATED ID: 1OIU RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH A 6-
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR
REMARK 900 RELATED ID: 1OIY RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/
REMARK 900 CYCLIN A COMPLEXED WITH A 6-
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR
REMARK 900 RELATED ID: 1OKV RELATED DB: PDB
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG-
REMARK 900 ARG-LEU-ILE-PHE-NH2
REMARK 900 RELATED ID: 1OKW RELATED DB: PDB
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR AC-ARG-
REMARK 900 ARG-LEU-ASN-(M-CL-PHE)-NH2
REMARK 900 RELATED ID: 1OL1 RELATED DB: PDB
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-CIT-
REMARK 900 CIT-LEU-ILE-(P-F-PHE)-NH2
REMARK 900 RELATED ID: 1OL2 RELATED DB: PDB
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG-
REMARK 900 ARG-LEU-ASN-(P-F-PHE)-NH2
REMARK 900 RELATED ID: 1P5E RELATED DB: PDB
REMARK 900 THE STRUCURE OF PHOSPHO-CDK2/CYCLIN A IN
REMARK 900 COMPLEX WITH THEINHIBITOR 4,5,6,7-
REMARK 900 TETRABROMOBENZOTRIAZOLE (TBS)
REMARK 900 RELATED ID: 1PKD RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF UCN-01 IN COMPLEX
REMARK 900 WITH PHOSPHO-CDK2/CYCLIN A
REMARK 900 RELATED ID: 1QMZ RELATED DB: PDB
REMARK 900 PHOSPHORYLATED CDK2-CYCLYIN A-SUBSTRATE
REMARK 900 PEPTIDE COMPLEX
REMARK 900 RELATED ID: 1URC RELATED DB: PDB
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG-
REMARK 900 ARG-LEU-ASN-(P-F-PHE)-NH2
REMARK 900 RELATED ID: 1VYW RELATED DB: PDB
REMARK 900 STRUCTURE OF CDK2/CYCLIN A WITH PNU-292137
REMARK 900 RELATED ID: 2BKZ RELATED DB: PDB
REMARK 900 STRUCTURE OF CDK2-CYCLIN A WITH PHA-404611
REMARK 900 RELATED ID: 2BPM RELATED DB: PDB
REMARK 900 STRUCTURE OF CDK2-CYCLIN A WITH PHA-630529
REMARK 900 RELATED ID: 2C4G RELATED DB: PDB
REMARK 900 STRUCTURE OF CDK2-CYCLIN A WITH PHA-533514
REMARK 900 RELATED ID: 2C5N RELATED DB: PDB
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE
REMARK 900 AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG
REMARK 900 DESIGN
REMARK 900 RELATED ID: 2C5O RELATED DB: PDB
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE
REMARK 900 AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG
REMARK 900 DESIGN
REMARK 900 RELATED ID: 2C5P RELATED DB: PDB
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE
REMARK 900 AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG
REMARK 900 DESIGN
REMARK 900 RELATED ID: 2C5T RELATED DB: PDB
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE
REMARK 900 AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG
REMARK 900 DESIGN
REMARK 900 RELATED ID: 2C5V RELATED DB: PDB
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE
REMARK 900 AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG
REMARK 900 DESIGN
REMARK 900 RELATED ID: 2C5X RELATED DB: PDB
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE
REMARK 900 AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG
REMARK 900 DESIGN
REMARK 900 RELATED ID: 2C6T RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2
REMARK 900 COMPLEXED WITH THE TRIAZOLOPYRIMIDINE INHIBITOR
REMARK 900 RELATED ID: 2CCH RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF CDK2 CYCLIN A IN
REMARK 900 COMPLEX WITH A SUBSTRATE PEPTIDE DERIVED
REMARK 900 FROM CDC MODIFIED WITH A GAMMA-LINKED ATP
REMARK 900 ANALOGUE
REMARK 900 RELATED ID: 2CCI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHO-CDK2 CYCLIN A
REMARK 900 IN COMPLEX WITH A PEPTIDE CONTAINING BOTH
REMARK 900 THE SUBSTRATE AND RECRUITMENT SITES OF CDC6
REMARK 900 RELATED ID: 2CJM RELATED DB: PDB
REMARK 900 MECHANISM OF CDK INHIBITION BY ACTIVE SITE
REMARK 900 PHOSPHORYLATION: CDK2 Y15P T160P IN COMPLEX
REMARK 900 WITH CYCLIN A STRUCTURE
REMARK 900 RELATED ID: 2IW6 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2-
REMARK 900 CYCLIN A COMPLEXED WITH A BISANILINOPYRIMIDINE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 2IW8 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2-
REMARK 900 CYCLIN A F82H-L83V-H84D MUTANT WITH AN
REMARK 900 O6-CYCLOHEXYLMETHYLGUANINE INHIBITOR
REMARK 900 RELATED ID: 2IW9 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2-
REMARK 900 CYCLIN A COMPLEXED WITH A BISANILINOPYRIMIDINE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 2UUE RELATED DB: PDB
REMARK 900 REPLACE: A STRATEGY FOR ITERATIVE DESIGN OF
REMARK 900 CYCLIN BINDING GROOVE INHIBITORS
REMARK 900 RELATED ID: 2UZB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 COMPLEXED
REMARK 900 WITH A THIAZOLIDINONE INHIBITOR
REMARK 900 RELATED ID: 2UZD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 COMPLEXED
REMARK 900 WITH A THIAZOLIDINONE INHIBITOR
REMARK 900 RELATED ID: 2UZL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 COMPLEXED
REMARK 900 WITH A THIAZOLIDINONE INHIBITOR
REMARK 900 RELATED ID: 2UZN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 COMPLEXED
REMARK 900 WITH A THIAZOLIDINONE INHIBITOR
REMARK 900 RELATED ID: 2UZO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 COMPLEXED
REMARK 900 WITH A THIAZOLIDINONE INHIBITOR
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 175 - 432 CYCLIN A2
DBREF 2UZE A 1 298 UNP P24941 CDK2_HUMAN 1 298
DBREF 2UZE B 175 432 UNP P20248 CCNA2_HUMAN 175 432
DBREF 2UZE C 1 298 UNP P24941 CDK2_HUMAN 1 298
DBREF 2UZE D 175 432 UNP P20248 CCNA2_HUMAN 175 432
SEQRES 1 A 298 MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY
SEQRES 2 A 298 THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR
SEQRES 3 A 298 GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR
SEQRES 4 A 298 GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE
SEQRES 5 A 298 SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS
SEQRES 6 A 298 LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU
SEQRES 7 A 298 VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET
SEQRES 8 A 298 ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE
SEQRES 9 A 298 LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE
SEQRES 10 A 298 CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO
SEQRES 11 A 298 GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU
SEQRES 12 A 298 ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL
SEQRES 13 A 298 ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR ARG
SEQRES 14 A 298 ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR
SEQRES 15 A 298 ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU
SEQRES 16 A 298 MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU
SEQRES 17 A 298 ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR
SEQRES 18 A 298 PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO
SEQRES 19 A 298 ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP
SEQRES 20 A 298 PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG
SEQRES 21 A 298 SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS
SEQRES 22 A 298 ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE
SEQRES 23 A 298 GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU
SEQRES 1 B 258 VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG
SEQRES 2 B 258 GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET
SEQRES 3 B 258 LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE
SEQRES 4 B 258 LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS
SEQRES 5 B 258 LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE
SEQRES 6 B 258 ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS
SEQRES 7 B 258 LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER
SEQRES 8 B 258 LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE
SEQRES 9 B 258 VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL
SEQRES 10 B 258 LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE
SEQRES 11 B 258 ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN
SEQRES 12 B 258 TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU
SEQRES 13 B 258 SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP
SEQRES 14 B 258 ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA
SEQRES 15 B 258 GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY
SEQRES 16 B 258 GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR
SEQRES 17 B 258 THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS
SEQRES 18 B 258 GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER
SEQRES 19 B 258 ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL
SEQRES 20 B 258 SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU
SEQRES 1 C 298 MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY
SEQRES 2 C 298 THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR
SEQRES 3 C 298 GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR
SEQRES 4 C 298 GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE
SEQRES 5 C 298 SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS
SEQRES 6 C 298 LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU
SEQRES 7 C 298 VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET
SEQRES 8 C 298 ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE
SEQRES 9 C 298 LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE
SEQRES 10 C 298 CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO
SEQRES 11 C 298 GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU
SEQRES 12 C 298 ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL
SEQRES 13 C 298 ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR ARG
SEQRES 14 C 298 ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR
SEQRES 15 C 298 ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU
SEQRES 16 C 298 MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU
SEQRES 17 C 298 ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR
SEQRES 18 C 298 PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO
SEQRES 19 C 298 ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP
SEQRES 20 C 298 PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG
SEQRES 21 C 298 SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS
SEQRES 22 C 298 ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE
SEQRES 23 C 298 GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU
SEQRES 1 D 258 VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG
SEQRES 2 D 258 GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET
SEQRES 3 D 258 LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE
SEQRES 4 D 258 LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS
SEQRES 5 D 258 LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE
SEQRES 6 D 258 ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS
SEQRES 7 D 258 LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER
SEQRES 8 D 258 LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE
SEQRES 9 D 258 VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL
SEQRES 10 D 258 LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE
SEQRES 11 D 258 ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN
SEQRES 12 D 258 TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU
SEQRES 13 D 258 SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP
SEQRES 14 D 258 ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA
SEQRES 15 D 258 GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY
SEQRES 16 D 258 GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR
SEQRES 17 D 258 THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS
SEQRES 18 D 258 GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER
SEQRES 19 D 258 ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL
SEQRES 20 D 258 SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU
MODRES 2UZE TPO A 160 THR PHOSPHOTHREONINE
MODRES 2UZE TPO C 160 THR PHOSPHOTHREONINE
HET TPO A 160 11
HET TPO C 160 11
HET C95 A1297 22
HET C95 C1297 22
HETNAM TPO PHOSPHOTHREONINE
HETNAM C95 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-
HETNAM 2 C95 YLIDENE)METHYL]FURAN-2-YL}BENZOIC ACID
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 TPO 2(C4 H10 N O6 P)
FORMUL 5 C95 2(C15 H10 N2 O4 S)
FORMUL 7 HOH *296(H2 O1)
HELIX 1 1 PRO A 45 LEU A 58 1 14
HELIX 2 2 LEU A 87 SER A 94 1 8
HELIX 3 3 PRO A 100 HIS A 121 1 22
HELIX 4 4 THR A 165 ARG A 169 5 5
HELIX 5 5 ALA A 170 LEU A 175 1 6
HELIX 6 6 THR A 182 ARG A 199 1 18
HELIX 7 7 SER A 207 GLY A 220 1 14
HELIX 8 8 GLY A 229 MET A 233 5 5
HELIX 9 9 ASP A 247 VAL A 252 1 6
HELIX 10 10 ASP A 256 LEU A 267 1 12
HELIX 11 11 SER A 276 ALA A 282 1 7
HELIX 12 12 HIS A 283 GLN A 287 5 5
HELIX 13 13 TYR B 178 CYS B 193 1 16
HELIX 14 14 GLY B 198 GLN B 203 5 6
HELIX 15 15 THR B 207 LYS B 226 1 20
HELIX 16 16 GLN B 228 MET B 246 1 19
HELIX 17 17 LEU B 249 GLY B 251 5 3
HELIX 18 18 LYS B 252 GLU B 269 1 18
HELIX 19 19 GLU B 274 THR B 282 1 9
HELIX 20 20 THR B 287 LEU B 302 1 16
HELIX 21 21 THR B 310 LEU B 320 1 11
HELIX 22 22 ASN B 326 ASP B 343 1 18
HELIX 23 23 ASP B 343 LEU B 348 1 6
HELIX 24 24 LEU B 351 GLY B 369 1 19
HELIX 25 25 PRO B 373 GLY B 381 1 9
HELIX 26 26 LEU B 387 ALA B 401 1 15
HELIX 27 27 PRO B 402 HIS B 404 5 3
HELIX 28 28 GLN B 407 TYR B 413 1 7
HELIX 29 29 LYS B 414 HIS B 419 5 6
HELIX 30 30 PRO C 45 GLU C 57 1 13
HELIX 31 31 LEU C 87 SER C 94 1 8
HELIX 32 32 PRO C 100 SER C 120 1 21
HELIX 33 33 LYS C 129 GLN C 131 5 3
HELIX 34 34 ASP C 145 ALA C 149 5 5
HELIX 35 35 THR C 165 ARG C 169 5 5
HELIX 36 36 ALA C 170 LEU C 175 1 6
HELIX 37 37 THR C 182 ARG C 199 1 18
HELIX 38 38 SER C 207 GLY C 220 1 14
HELIX 39 39 GLY C 229 MET C 233 5 5
HELIX 40 40 ASP C 247 VAL C 252 1 6
HELIX 41 41 ASP C 256 LEU C 267 1 12
HELIX 42 42 SER C 276 LEU C 281 1 6
HELIX 43 43 HIS C 283 GLN C 287 5 5
HELIX 44 44 TYR D 178 CYS D 193 1 16
HELIX 45 45 THR D 207 TYR D 225 1 19
HELIX 46 46 GLN D 228 MET D 246 1 19
HELIX 47 47 LEU D 249 GLY D 251 5 3
HELIX 48 48 LYS D 252 GLU D 269 1 18
HELIX 49 49 GLU D 274 THR D 282 1 9
HELIX 50 50 THR D 287 LEU D 302 1 16
HELIX 51 51 THR D 310 LEU D 320 1 11
HELIX 52 52 ASN D 326 ASP D 343 1 18
HELIX 53 53 ASP D 343 LEU D 348 1 6
HELIX 54 54 LEU D 351 GLY D 369 1 19
HELIX 55 55 PRO D 373 GLY D 381 1 9
HELIX 56 56 THR D 383 ALA D 401 1 19
HELIX 57 57 PRO D 402 HIS D 404 5 3
HELIX 58 58 GLN D 407 TYR D 413 1 7
HELIX 59 59 LYS D 414 HIS D 419 5 6
HELIX 60 60 GLY D 420 LEU D 424 5 5
SHEET 1 AA 5 PHE A 4 GLU A 12 0
SHEET 2 AA 5 VAL A 17 ASN A 23 -1 O VAL A 18 N ILE A 10
SHEET 3 AA 5 VAL A 29 ARG A 36 -1 O VAL A 30 N ALA A 21
SHEET 4 AA 5 LYS A 75 GLU A 81 -1 O LEU A 76 N ILE A 35
SHEET 5 AA 5 LEU A 66 HIS A 71 -1 N LEU A 67 O VAL A 79
SHEET 1 AB 3 GLN A 85 ASP A 86 0
SHEET 2 AB 3 LEU A 133 ILE A 135 -1 O ILE A 135 N GLN A 85
SHEET 3 AB 3 ILE A 141 LEU A 143 -1 O LYS A 142 N LEU A 134
SHEET 1 AC 2 VAL A 123 LEU A 124 0
SHEET 2 AC 2 ARG A 150 ALA A 151 -1 O ARG A 150 N LEU A 124
SHEET 1 CA 5 PHE C 4 GLU C 12 0
SHEET 2 CA 5 VAL C 17 ASN C 23 -1 O VAL C 18 N ILE C 10
SHEET 3 CA 5 VAL C 29 ARG C 36 -1 O VAL C 30 N ALA C 21
SHEET 4 CA 5 LYS C 75 GLU C 81 -1 O LEU C 76 N ILE C 35
SHEET 5 CA 5 LEU C 66 HIS C 71 -1 N LEU C 67 O VAL C 79
SHEET 1 CB 3 GLN C 85 ASP C 86 0
SHEET 2 CB 3 LEU C 133 ILE C 135 -1 O ILE C 135 N GLN C 85
SHEET 3 CB 3 ILE C 141 LEU C 143 -1 O LYS C 142 N LEU C 134
SHEET 1 CC 2 VAL C 123 LEU C 124 0
SHEET 2 CC 2 ARG C 150 ALA C 151 -1 O ARG C 150 N LEU C 124
LINK C TYR A 159 N TPO A 160 1555 1555 1.33
LINK C TPO A 160 N HIS A 161 1555 1555 1.33
LINK C TYR C 159 N TPO C 160 1555 1555 1.33
LINK C TPO C 160 N HIS C 161 1555 1555 1.33
CISPEP 1 VAL A 154 PRO A 155 0 -4.30
CISPEP 2 GLN B 323 PRO B 324 0 -12.62
CISPEP 3 ASP B 345 PRO B 346 0 10.50
CISPEP 4 VAL C 154 PRO C 155 0 -12.66
CISPEP 5 GLN D 323 PRO D 324 0 -9.42
CISPEP 6 ASP D 345 PRO D 346 0 9.62
SITE 1 AC1 14 ILE A 10 GLY A 13 ALA A 31 LYS A 33
SITE 2 AC1 14 GLU A 51 PHE A 80 GLU A 81 LEU A 83
SITE 3 AC1 14 HIS A 84 GLN A 85 ASP A 86 LYS A 89
SITE 4 AC1 14 LEU A 134 ASP A 145
SITE 1 AC2 13 ILE C 10 GLY C 13 ALA C 31 LYS C 33
SITE 2 AC2 13 PHE C 80 GLU C 81 LEU C 83 HIS C 84
SITE 3 AC2 13 ASP C 86 LYS C 89 LEU C 134 ASP C 145
SITE 4 AC2 13 HOH C2010
CRYST1 212.626 73.436 153.028 90.00 129.54 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004703 0.000000 0.003882 0.00000
SCALE2 0.000000 0.013617 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008474 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
